Natural Alpha-Glucosidase Inhibitors: Therapeutic Implication and Structure- Activity Relation Ship

Title:Natural Alpha-Glucosidase Inhibitors: Therapeutic Implication and Structure- Activity Relation Ship

Volume: 13 Issue: 7

Author(s): Sanae Abid, Ali Berraaouan and Mohamed Bnouham

Affiliation:

Keywords: α-glucosidase inhibitors, diseases, chemical structure, natural product, structure-activity relationship.

Abstract: Background: Alpha-glucosidase is the key enzyme involved in catalyzing the carbohydrate alpha-glucosidase through hydrolysis. It is implicated in several metabolic pathways, including carbohydrate digestion in the intestine, and glycoprotein and glycolipid processing. Alpha-glucosidase inhibitors are currently being investigated for their therapeutic effect against some diseases such as diabetes, cancer, hepatitis B and human immunodeficiency virus (HIV).

Objective: The aim of this review is to clarify the effect of alpha-glucosidase inhibitors in the treatment of some diseases, and to evaluate the structure-activity relationship of about 270 inhibitors isolated from about 60 plants.

Methods: We reviewed 121 articles published between 1965 and 2013 (PubMed and Sciencedirect). All the molecules structures were provided in ChemDraw software.

Results and Conclusions: In this work we elucidated the therapeutic effect of alpha-glucosidase inhibitors against some diseases and we concluded that alpha-glucosidase flavonoid inhibitors (representing 22% of the reviewed inhibitors) have common components that are responsible of their inhibitory activity. The general structure of these inhibitors is composed of three rings. It seems that the hydroxyl groups in each ring have an important role in the α-glucosidase inhibitory activity.

Cite this article as:

Abid Sanae, Berraaouan Ali and Bnouham Mohamed, Natural Alpha-Glucosidase Inhibitors: Therapeutic Implication and Structure- Activity Relation Ship, Letters in Drug Design & Discovery 2016; 13 (7) . https://dx.doi.org/10.2174/1570180812666150918193508